Identification of the Chromophores Involved in Aggregation-dependent Energy Quenching of the Monomeric Photosystem II Antenna Protein Lhcb5

被引:29
作者
Ballottari, Matteo [1 ]
Girardon, Julien [1 ]
Betterle, Nico [1 ]
Morosinotto, Tomas [2 ]
Bassi, Roberto [1 ]
机构
[1] Univ Verona, Dipartimento Biotecnol, I-37134 Verona, Italy
[2] Univ Padua, Dipartimento Biol, I-35121 Padua, Italy
关键词
LIGHT-HARVESTING-COMPLEX; TIME-RESOLVED FLUORESCENCE; PIGMENT-PIGMENT INTERACTIONS; A/B BINDING-PROTEINS; FAR-RED FLUORESCENCE; HIGHER-PLANT ANTENNA; CHLOROPHYLL FLUORESCENCE; MUTATION ANALYSIS; IN-VITRO; ELECTRON CRYSTALLOGRAPHY;
D O I
10.1074/jbc.M110.124115
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Non-photochemical quenching (NPQ) of excess absorbed light energy is a fundamental process that regulates photosynthetic light harvesting in higher plants. Among several proposed NPQ mechanisms, aggregation-dependent quenching (ADQ) and charge transfer quenching have received the most attention. In vitro spectroscopic features of both mechanisms correlate with very similar signals detected in more intact systems and in vivo, where full NPQ can be observed. A major difference between the models is the proposed quenching site, which is predominantly the major trimeric light-harvesting complex II in ADQ and exclusively monomeric Lhcb proteins in charge transfer quenching. Here, we studied ADQ in both monomeric and trimeric Lhcb proteins, investigating the activities of each antenna subunit and their dependence on zeaxanthin, a major modulator of NPQ in vivo. We found that monomeric Lhcb proteins undergo stronger quenching than light-harvesting complex II during aggregation and that this is enhanced by binding to zeaxanthin, as occurs during NPQ in vivo. Finally, the analysis of Lhcb5 mutants showed that chlorophyll 612 and 613, in close contact with lutein bound at site L1, are important facilitators of ADQ.
引用
收藏
页码:28309 / 28321
页数:13
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